Journal of Applied Physiology
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J Appl Physiol 89: 695-703, 2000;
8750-7587/00 $5.00
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Vol. 89, Issue 2, 695-703, August 2000

Maximum specific force depends on myosin heavy chain content in rat diaphragm muscle fibers

Paige C. Geiger, Mark J. Cody, Rebecca L. Macken, and Gary C. Sieck

Departments of Anesthesiology and of Physiology and Biophysics, Mayo Clinic and Foundation, Rochester, Minnesota 55905

In the present study, myosin heavy chain (MHC) content per half sarcomere, an estimate of the number of cross bridges available for force generation, was determined in rat diaphragm muscle (Diam) fibers expressing different MHC isoforms. We hypothesize that fiber-type differences in maximum specific force [force per cross-sectional area (CSA)] reflect the number of cross bridges present per CSA. Studies were performed on single, Triton X-100-permeabilized rat Diam fibers. Maximum specific force was determined by activation of single Diam fibers in the presence of a high-calcium solution (pCa, -log Ca2+ concentration of 4.0). SDS-PAGE and Western blot analyses were used to determine MHC isoform composition and MHC content per half sarcomere. Differences in maximum specific force across fast MHC isoforms were eliminated when controlled for half-sarcomere MHC content. However, the force produced by slow fibers remained below that of fast fibers when normalized for the number of cross bridges available. On the basis of these results, the lower force produced by slow fibers may be due to less force per cross bridge compared with fast fibers.

skinned fibers; force per cross bridge; fiber morphometry


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